-
When acid dissolves in water, they release __
hydrogen ions: H+ (protons)
-
Bases __ H+ ions
accepts
(H+ ions can attach to other molecules & change their properties)
-
pH is the measure of __
hydrogen ion concentration (H+)
-
The pH scale indicates __
the strength of a solution of an acid or base
(A pH of 7 means the concentration of H+ ions is 1 x 10^-7 of water)
(page 41 on slide)
-
4 major types of biological molecules
- proteins
- carbohydrates
- lipids
- nucleic acids
(All are polymers except lipids)
-
Proteins are combinations of __
20 amino acids
-
Carbs are __ linked to form __
sugar monomers (monosaccharides); polysaccharides
-
Nucleic acids are made up of __
4 kinds of nucleotide monomers
i.e. DNA & RNA
-
Lipids: __ forces maintain interactions between __
Noncovalent; lipid monomers
(phospholipid makes up cell membrane)
-
Out of the types of macromolecules, our body contains mostly __
protein (polypeptides)
(page 44 on slide)
-
Condensation (Dehydration Synthesis)
2 monomers produce a polymer (forms bonds)
(page 45 on slide)
-
Hydrolysis
Polymer splits into monomers
(page 46 on slide)
-
types of proteins (functions)
- enzymes: accelerate (catalyze) reactions
- defensive proteins (antibodies)
- hormonal & regulatory proteins
- receptor proteins: monitor cellular activity
- storage, structure, transport
- genetic regulatory proteins
-
__ are NOT done by proteins
energy & information storage
-
__ determines the structure of proteins
The primary amino acid sequence
-
The amino acid structure is made up of __
- carbon
- hydrogen
- amino group (H3N+)
- carboxyl group (COO-)
- side chain (R)
(page 48 on slide)
-
Amino acids with polar side chains are __
hydrophilic (charged & uncharged)
(page 49 & 50 on slide)
-
Amino acids with nonpolar uncharged side chains are __
hydrophobic
(page 51 on slide)
-
amino acid special cases
- Cysteine (Cys)
- Glycine (Gly)
- Proline (Pro)
(page 52 on slide)
-
Cysteine
forms disulfide bonds which affects the 3D structure of the protein
side chain: CH2-SH
(page 53 on slide)
-
Glycine
- small, fits in tight corners
- serves as a neurotransmitter
side chain: H
(page 54 on slide)
-
Proline
found at bends & loops
side chain (connects to carbon & amino group): CH2-CH2-CH2
(page 55 on slide)
-
Amino acids bond together covalently in a __ reaction by __ linkages/bonds
condensation (dehydration synthesis); peptide
(page 56 on slide)
-
The first amino acid in a polypeptide is the __ terminus, whereas the last amino acid in a polypeptide is the __ terminus
N; C
(page 57 on slide)
-
The primary protein structure is determined by __ bonds and and the secondary structure is determined by __ bonds
peptide; hydrogen (H)
-
primary level of protein structure
the sequence of amino acids in a polypeptide
(page 59 on slide)
-
secondary level of protein structure: alpha helix
H-Bonds form between the hydrogen of one amino acid & oxygen of another amino acid
(page 60 on slide)
-
secondary level of protein structure: beta pleated sheet
H-bonds form between hydrogen & oxygen, but in a side-by-side arrangement.
(This can be the same polypeptide folded back on itself, or 2 different polypeptides.)
(page 61 on slide)
-
tertiary level of protein structure
Bending & folding results in a macromolecule with specific 3D shape.
The outer surfaces present functional groups that can interact with other molecules.
(page 63 on slide)
-
Tertiary structure (of protein) is determined by interactions of __
R-groups:
- disulfide bridges
- hydrogen bonds
- aggregation of hydrophobic side chains
- van der Waal forces
- ionic bonds
-
quaternary level of protein structure
results from the interaction of subunits of hydrophobic interactions, van der Waal forces, ionic bonds, & hydrogen bonds
Each subunit has its own unique tertiary structure
example: hemoglobin
(page 66 on slide)
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